Show simple item record

dc.creatorNikodinović-Runić, Jasmina
dc.creatorCoulombel, Lydie
dc.creatorFrancuski, Đorđe
dc.creatorSharma, Narain D.
dc.creatorBoyd, Derek R.
dc.creatorFerrall, Rory Moore O.
dc.creatorO'Connor, Kevin E.
dc.date.accessioned2018-11-22T00:23:12Z
dc.date.available2018-11-22T00:23:12Z
dc.date.issued2013
dc.identifier.issn0175-7598
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/1355
dc.description.abstractNine different sulfur-containing compounds were biotransformed to the corresponding sulfoxides by Escherichia coli Bl21(DE3) cells expressing styrene monooxygenase (SMO) from Pseudomonas putida CA-3. Thioanisole was consumed at 83.3 mu moles min(-1) g cell dry weight(-1) resulting mainly in the formation of R-thioanisole sulfoxide with an enantiomeric excess (ee) value of 45 %. The rate of 2-methyl-, 2-chloro- and 2-bromo-thioanisole consumption was 2-fold lower than that of thioanisole. Surprisingly, the 2-methylthioanisole sulfoxide product had the opposite (S) configuration to that of the other 2-substituted thioanisole derivatives and had a higher ee value (84 %). The rate of oxidation of 4-substituted thioanisoles was higher than the corresponding 2-substituted substrates but the ee values of the products were consistently lower (10-23 %). The rate of benzo[b]thiophene and 2-methylbenzo[b]thiophene sulfoxidation was approximately 10-fold lower than that of thioanisole. The ee value of the benzo[b]thiophene sulfoxide could not be determined as the product racemized rapidly. E. coli cells expressing an engineered SMO (SMOeng R3-11) oxidised 2-substituted thioanisoles between 1.8- and 2.8-fold faster compared to cells expressing the wild-type enzyme. SMOeng R3-11 oxidised benzo[b]thiophene and 2-methylbenzo[b]thiophene 10.1 and 5.6 times faster that the wild-type enzyme. The stereospecificity of the reaction catalysed by SMOeng was unchanged from that of the wild type. Using the X-ray crystal structure of the P. putida S12 SMO, it was evident that the entrance of substrates into the SMO active site is limited by the binding pocket bottleneck formed by the side chains of Val-211 and Asn-46 carboxyamide group.en
dc.publisherSpringer, New York
dc.rightsrestrictedAccess
dc.sourceApplied Microbiology and Biotechnology
dc.subjectBiotransformationen
dc.subjectStyrene monooxygenaseen
dc.subjectAlkyaryl suphidesen
dc.subjectBenzo[b]thiophenesen
dc.subjectSulfoxidationen
dc.titleThe oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3en
dc.typearticle
dc.rights.licenseARR
dcterms.abstractФерралл, Рорy Мооре О.; О'Цоннор, Кевин Е.; Никодиновић-Рунић, Јасмина; Схарма, Нараин Д.; Боyд, Дерек Р.; Француски, Дјордје; Цоуломбел, Лyдие;
dc.citation.volume97
dc.citation.issue11
dc.citation.spage4849
dc.citation.epage4858
dc.identifier.wos000319136300015
dc.identifier.doi10.1007/s00253-012-4332-5
dc.citation.other97(11): 4849-4858
dc.citation.rankM21
dc.identifier.pmid22890778
dc.type.versionpublishedVersionen
dc.identifier.scopus2-s2.0-84878016310
dc.identifier.rcubKon_2475


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record